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Q4JHE3

- OXLA_OXYSC

UniProt

Q4JHE3 - OXLA_OXYSC

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Protein
L-amino-acid oxidase
Gene
N/A
Organism
Oxyuranus scutellatus scutellatus (Australian taipan) (Coastal taipan)
Status
Reviewed - Annotation score: 3 out of 5 - Experimental evidence at transcript leveli

Functioni

Catalyzes an oxidative deamination of predominantly hydrophobic and aromatic L-amino acids, thus producing hydrogen peroxide that may contribute to the diverse toxic effects of this enzyme. Exhibits diverse biological activities, such as hemorrhage, hemolysis, edema, apoptosis of vascular endothelial cells or tumor cell lines, antibacterial and antiparasitic activities, as well as regulation of platelet aggregation. Effects of snake L-amino oxidases on platelets are controversial, since they either induce aggregation or inhibit agonist-induced aggregation. These different effects are probably due to different experimental conditions By similarity.

Catalytic activityi

An L-amino acid + H2O + O2 = a 2-oxo acid + NH3 + H2O2.

Cofactori

FAD By similarity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei90 – 901FAD By similarity
Binding sitei109 – 1091Substrate By similarity
Binding sitei280 – 2801FAD; via amide nitrogen and carbonyl oxygen By similarity
Binding sitei391 – 3911Substrate By similarity
Binding sitei476 – 4761FAD By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi62 – 632FAD By similarity
Nucleotide bindingi82 – 832FAD By similarity
Nucleotide bindingi106 – 1094FAD By similarity
Nucleotide bindingi483 – 4886FAD By similarity
Nucleotide bindingi483 – 4842Substrate By similarity

GO - Molecular functioni

  1. L-amino-acid oxidase activity Source: UniProtKB-EC

GO - Biological processi

  1. apoptotic process Source: UniProtKB-KW
  2. defense response to bacterium Source: UniProtKB-KW
  3. hemolysis in other organism Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Antibiotic, Antimicrobial, Hemostasis impairing toxin, Oxidoreductase, Toxin

Keywords - Biological processi

Apoptosis, Cytolysis, Hemolysis

Keywords - Ligandi

FAD, Flavoprotein

Names & Taxonomyi

Protein namesi
Recommended name:
L-amino-acid oxidase (EC:1.4.3.2)
Short name:
LAAO
Short name:
LAO
OrganismiOxyuranus scutellatus scutellatus (Australian taipan) (Coastal taipan)
Taxonomic identifieri8667 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataBifurcataUnidentataEpisquamataToxicoferaSerpentesColubroideaElapidaeAcanthophiinaeOxyuranus

Subcellular locationi

Secreted By similarity

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1818 By similarity
Add
BLAST
Chaini19 – 517499L-amino-acid oxidase
PRO_5000140378Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi29 ↔ 192 By similarity
Glycosylationi191 – 1911N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi350 ↔ 431 By similarity
Glycosylationi380 – 3801N-linked (GlcNAc...) Reviewed prediction

Post-translational modificationi

N-glycosylated By similarity.

Keywords - PTMi

Disulfide bond, Glycoprotein

Expressioni

Tissue specificityi

Expressed by the venom gland.

Interactioni

Subunit structurei

Homodimer; non-covalently linked By similarity.

Structurei

3D structure databases

ProteinModelPortaliQ4JHE3.
SMRiQ4JHE3. Positions 23-505.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

HOVERGENiHBG005729.

Family and domain databases

InterProiIPR002937. Amino_oxidase.
IPR001613. Flavin_amine_oxidase.
[Graphical view]
PfamiPF01593. Amino_oxidase. 1 hit.
[Graphical view]
PRINTSiPR00757. AMINEOXDASEF.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q4JHE3-1 [UniParc]FASTAAdd to Basket

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MNVFFMFSLL FLAALESCAD VRRNPLEECF READYEEFLE IARNGLKKTS    50
NPKHVVVVGA GMAGLSAAYV LAGAGHKVTL LEASERVGGR VHTYRNEKEG 100
WYVNLGPMRL PERHRIIREY IRKFGLKLNE FFQENENAWY FIRNIRKRVW 150
EVKKDPGVFK YPVKPSEEGK SASQLYRESL KKVIEELKRT NCSYILNKYD 200
TYSTKEYLIK EGNLSRGAVD MIGDLLNEDS SYYLSFIESL KSDDLFSYEK 250
RFDEIVGGFD QLPISMYQAI AEMVHLNAQV IKIQHNAEKV RVAYQTPAKT 300
LSYVTADYVI VCSSSRAARR IYFEPPLPPK KAHALRSIHY KSGTKIFLTC 350
SKKFWEADGI HGGKSTTDLP SRFIYYPNHN FTSGVGVIVA YTISDDADFF 400
QSLDIKTSAD IVINDLSLIH QLPKKEIQAL CYPSMIKKWS LDKYAMGSIT 450
SFAPYQFQDF IERVAAPVGR IYFAGEYTAR VHGWLDSTIK SGLTAARDVN 500
RASQKPSRRQ LSNDNEL 517
Length:517
Mass (Da):59,070
Last modified:August 2, 2005 - v1
Checksum:i1509F4998BFD08A2
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
DQ088990 mRNA. Translation: AAY89680.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
DQ088990 mRNA. Translation: AAY89680.1 .

3D structure databases

ProteinModelPortali Q4JHE3.
SMRi Q4JHE3. Positions 23-505.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

HOVERGENi HBG005729.

Family and domain databases

InterProi IPR002937. Amino_oxidase.
IPR001613. Flavin_amine_oxidase.
[Graphical view ]
Pfami PF01593. Amino_oxidase. 1 hit.
[Graphical view ]
PRINTSi PR00757. AMINEOXDASEF.
ProtoNeti Search...

Publicationsi

  1. "Identification and analysis of venom gland-specific genes from the coastal taipan (Oxyuranus scutellatus) and related species."
    St Pierre L., Woods R., Earl S.T.H., Masci P.P., Lavin M.F.
    Cell. Mol. Life Sci. 62:2679-2693(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Venom gland.

Entry informationi

Entry nameiOXLA_OXYSC
AccessioniPrimary (citable) accession number: Q4JHE3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 23, 2007
Last sequence update: August 2, 2005
Last modified: February 19, 2014
This is version 47 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programAnimal Toxin Annotation Program
Annotation programChordata Protein Annotation Program

Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi